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D4ZVW7

- D4ZVW7_ARTPN

UniProt

D4ZVW7 - D4ZVW7_ARTPN

Protein

Ribulose bisphosphate carboxylase large chain

Gene

cbbL

Organism
Arthrospira platensis (strain NIES-39 / IAM M-135) (Spirulina platensis)
Status
Unreviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 23 (01 Oct 2014)
      Sequence version 1 (15 Jun 2010)
      Previous versions | rss
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    Functioni

    RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.UniRule annotation

    Catalytic activityi

    2 3-phospho-D-glycerate + 2 H+ = D-ribulose 1,5-bisphosphate + CO2 + H2O.UniRule annotation
    3-phospho-D-glycerate + 2-phosphoglycolate = D-ribulose 1,5-bisphosphate + O2.UniRule annotation

    Cofactori

    Binds 1 magnesium ion per subunit.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei124 – 1241Substrate; in homodimeric partnerUniRule annotation
    Binding sitei174 – 1741SubstrateUniRule annotation
    Active sitei176 – 1761Proton acceptorUniRule annotation
    Binding sitei178 – 1781SubstrateUniRule annotation
    Metal bindingi202 – 2021Magnesium; via carbamate groupUniRule annotation
    Metal bindingi204 – 2041MagnesiumUniRule annotation
    Metal bindingi205 – 2051MagnesiumUniRule annotation
    Active sitei295 – 2951Proton acceptorUniRule annotation
    Binding sitei296 – 2961SubstrateUniRule annotation
    Binding sitei328 – 3281SubstrateUniRule annotation
    Sitei335 – 3351Transition state stabilizerUniRule annotation
    Binding sitei380 – 3801SubstrateUniRule annotation

    GO - Molecular functioni

    1. magnesium ion binding Source: UniProtKB-HAMAP
    2. monooxygenase activity Source: UniProtKB-KW
    3. ribulose-bisphosphate carboxylase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. photorespiration Source: UniProtKB-KW
    2. reductive pentose-phosphate cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    LyaseUniRule annotation, MonooxygenaseUniRule annotation, Oxidoreductase

    Keywords - Biological processi

    Calvin cycleUniRule annotation, Carbon dioxide fixationUniRule annotation, PhotorespirationUniRule annotation

    Keywords - Ligandi

    MagnesiumUniRule annotation, Metal-bindingUniRule annotation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ribulose bisphosphate carboxylase large chainUniRule annotation (EC:4.1.1.39UniRule annotation)
    Short name:
    RuBisCO large subunitUniRule annotation
    Gene namesi
    Name:cbbLUniRule annotation
    Synonyms:rbcLUniRule annotation
    ORF Names:NIES39_K02850Imported
    OrganismiArthrospira platensis (strain NIES-39 / IAM M-135) (Spirulina platensis)Imported
    Taxonomic identifieri696747 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeOscillatorialesArthrospira
    ProteomesiUP000006803: Chromosome

    PTM / Processingi

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei202 – 2021N6-carboxylysineUniRule annotation
    Disulfide bondi248 – 248Interchain; in linked formUniRule annotation

    Post-translational modificationi

    The disulfide bond which can form in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover.UniRule annotation

    Keywords - PTMi

    Disulfide bondUniRule annotation

    Interactioni

    Subunit structurei

    Heterohexadecamer of 8 large chains and 8 small chains; disulfide-linked. The disulfide link is formed within the large subunit homodimers.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliD4ZVW7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RuBisCO large chain family. Type I subfamily.UniRule annotation

    Phylogenomic databases

    KOiK01601.

    Family and domain databases

    Gene3Di3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    HAMAPiMF_01338. RuBisCO_L_type1.
    InterProiIPR020878. RuBisCo_large_chain_AS.
    IPR020888. RuBisCO_lsu.
    IPR000685. RuBisCO_lsu_C.
    IPR017443. RuBisCO_lsu_fd_N.
    IPR017444. RuBisCO_lsu_N.
    [Graphical view]
    PfamiPF00016. RuBisCO_large. 1 hit.
    PF02788. RuBisCO_large_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF51649. SSF51649. 1 hit.
    SSF54966. SSF54966. 1 hit.
    PROSITEiPS00157. RUBISCO_LARGE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    D4ZVW7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSYSQTQTKS KAGYQAGVKD YKLTYYTPDY TPKDTDILAA FRVSPQPGVP    50
    PEEAGAAVAA ESSTGTWTTV WTDLLTDLDR YKGRCYHIEP VPGEDNQFFC 100
    FVAYPLDLFE EGSVTNMLTS IVGNVFGFKA LRGLRLEDMR IPIAYLKTFQ 150
    GPPHGITVER DKLNKYGRPL LGCTIKPKLG LSAKNYGRAV YECLRGGLDF 200
    TKDDENINSQ PFMRWRDRFL FVQEAIEKAQ AETNEIKGHY LNVTAPTCEE 250
    MMKRAEFAKE IGTPIIMHDF FTAGFTANTT LARWCRDNGL LLHIHRAMHA 300
    VVDRQRNHGI HFRVLAKCLR MSGGDHLHSG TVVGKLEGEK GITMGFVDLM 350
    REDHIEEDRS RGIFFTQDWA SMPGVMPVAS GGIHVWHMPA LVEIFGDDSC 400
    LQFGGGTLGH PWGNAPGATA NRVALEACIQ ARNEGRNLFR EGGDVIREAC 450
    KWSPELAVAC ELWKEIKFEF EAMDTL 476
    Length:476
    Mass (Da):53,280
    Last modified:June 15, 2010 - v1
    Checksum:iBFC00F25F64B695A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP011615 Genomic DNA. Translation: BAI91932.1.
    RefSeqiWP_006620100.1. NC_016640.1.
    YP_005070470.1. NC_016640.1.

    Genome annotation databases

    EnsemblBacteriaiBAI91932; BAI91932; NIES39_K02850.
    GeneIDi15167013.
    KEGGiarp:NIES39_K02850.
    PATRICi42721513. VBIArtPla153080_1977.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP011615 Genomic DNA. Translation: BAI91932.1 .
    RefSeqi WP_006620100.1. NC_016640.1.
    YP_005070470.1. NC_016640.1.

    3D structure databases

    ProteinModelPortali D4ZVW7.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAI91932 ; BAI91932 ; NIES39_K02850 .
    GeneIDi 15167013.
    KEGGi arp:NIES39_K02850.
    PATRICi 42721513. VBIArtPla153080_1977.

    Phylogenomic databases

    KOi K01601.

    Family and domain databases

    Gene3Di 3.20.20.110. 1 hit.
    3.30.70.150. 1 hit.
    HAMAPi MF_01338. RuBisCO_L_type1.
    InterProi IPR020878. RuBisCo_large_chain_AS.
    IPR020888. RuBisCO_lsu.
    IPR000685. RuBisCO_lsu_C.
    IPR017443. RuBisCO_lsu_fd_N.
    IPR017444. RuBisCO_lsu_N.
    [Graphical view ]
    Pfami PF00016. RuBisCO_large. 1 hit.
    PF02788. RuBisCO_large_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51649. SSF51649. 1 hit.
    SSF54966. SSF54966. 1 hit.
    PROSITEi PS00157. RUBISCO_LARGE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NIES-39 / IAM M-135Imported.

    Entry informationi

    Entry nameiD4ZVW7_ARTPN
    AccessioniPrimary (citable) accession number: D4ZVW7
    Entry historyi
    Integrated into UniProtKB/TrEMBL: June 15, 2010
    Last sequence update: June 15, 2010
    Last modified: October 1, 2014
    This is version 23 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Miscellaneous

    The basic functional RuBisCO is composed of a large chain homodimer in a "head-to-tail" conformation. In form I RuBisCO this homodimer is arranged in a barrel-like tetramer with the small subunits forming a tetrameric "cap" on each end of the "barrel".UniRule annotation

    Keywords - Technical termi

    Complete proteome, Reference proteomeImported

    External Data

    Dasty 3